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Quinacrine acts as an antioxidant and reduces the toxicity of the prion peptide PrP106-126.

Research output: Contribution to journalJournal article


<mark>Journal publication date</mark>15/09/2003
Number of pages3
<mark>Original language</mark>English


The accumulation of protein aggregates in the brain is a central feature of several different neurodegenerative diseases. We have recently shown that A[beta] and [alpha]-synuclein, associated with Alzheimer's disease, Parkinson's disease and related disorders, can both induce the formation of hydroxyl radicals following incubation in solution, upon addition of Fe(II). PrP106-126, a model peptide for the study of prion protein-mediated cell death, shares the same property. In this study we show that quinacrine (an anti-malarial drug and inhibitor of prion replication) acts as an effective antioxidant, readily scavenging hydroxyl radicals formed from hydrogen peroxide via the Fenton reaction or generated during incubation of the PrP106-126 peptide. Furthermore, the toxicity of PrP106-126 to cultured cells was significantly inhibited by quinacrine.